相似文献
1
Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis.
Protein Sci. 2006 Jun;15(6):1270-6. doi: 10.1110/ps.062100606. Epub 2006 May 2.
2
Nucleotide-induced transition of GroEL from the high-affinity to the low-affinity state for a target protein: effects of ATP and ADP on the GroEL-affected refolding of alpha-lactalbumin.
J Mol Biol. 2001 Sep 21;312(3):555-67. doi: 10.1006/jmbi.2001.4959.
3
Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.
Science. 1995 Aug 11;269(5225):836-41. doi: 10.1126/science.7638601.
4
Allosteric control by ATP of non-folded protein binding to GroEL.
J Mol Biol. 1996 Jan 26;255(3):356-61. doi: 10.1006/jmbi.1996.0028.
5
Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings.
J Mol Biol. 1998 Apr 24;278(1):267-78. doi: 10.1006/jmbi.1998.1704.
6
Triggering protein folding within the GroEL-GroES complex.
J Biol Chem. 2008 Nov 14;283(46):32003-13. doi: 10.1074/jbc.M802898200. Epub 2008 Sep 9.
7
Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.
Proc Natl Acad Sci U S A. 2004 Oct 19;101(42):15005-12. doi: 10.1073/pnas.0406132101. Epub 2004 Oct 12.
8
A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL.
J Mol Biol. 1999 Oct 29;293(3):667-84. doi: 10.1006/jmbi.1999.3138.
9
Residues in chaperonin GroEL required for polypeptide binding and release.
Nature. 1994 Oct 13;371(6498):614-9. doi: 10.1038/371614a0.
10
Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP.
Biochim Biophys Acta. 2001 Feb 9;1545(1-2):160-73. doi: 10.1016/s0167-4838(00)00274-0.
引用本文的文献
1
Reduced ADP off-rate by the yeast CCT2 double mutation T394P/R510H which causes Leber congenital amaurosis in humans.
Commun Biol. 2023 Aug 29;6(1):888. doi: 10.1038/s42003-023-05261-8.
2
Signalling networks and dynamics of allosteric transitions in bacterial chaperonin GroEL: implications for iterative annealing of misfolded proteins.
Philos Trans R Soc Lond B Biol Sci. 2018 Jun 19;373(1749). doi: 10.1098/rstb.2017.0182.
3
Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange.
Proc Natl Acad Sci U S A. 2013 Nov 12;110(46):E4289-97. doi: 10.1073/pnas.1317702110. Epub 2013 Oct 28.
4
Putting handcuffs on the chaperonin GroEL.
Proc Natl Acad Sci U S A. 2013 Jul 2;110(27):10884-5. doi: 10.1073/pnas.1309581110. Epub 2013 Jun 19.
5
ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin.
Cell. 2012 Mar 30;149(1):113-23. doi: 10.1016/j.cell.2012.02.047. Epub 2012 Mar 22.
6
Out-of-equilibrium conformational cycling of GroEL under saturating ATP concentrations.
Proc Natl Acad Sci U S A. 2010 Apr 6;107(14):6270-4. doi: 10.1073/pnas.0910246107. Epub 2010 Mar 22.
7
Perturbation-based Markovian transmission model for probing allosteric dynamics of large macromolecular assembling: a study of GroEL-GroES.
PLoS Comput Biol. 2009 Oct;5(10):e1000526. doi: 10.1371/journal.pcbi.1000526. Epub 2009 Oct 2.
8
The GroEL/GroES cis cavity as a passive anti-aggregation device.
FEBS Lett. 2009 Aug 20;583(16):2654-62. doi: 10.1016/j.febslet.2009.06.049. Epub 2009 Jul 3.
9
Allosteric transitions in biological nanomachines are described by robust normal modes of elastic networks.
Curr Protein Pept Sci. 2009 Apr;10(2):128-32. doi: 10.2174/138920309787847608.
10
Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.
Proc Natl Acad Sci U S A. 2008 Nov 11;105(45):17334-8. doi: 10.1073/pnas.0807429105. Epub 2008 Nov 6.
本文引用的文献
1
Crystal structure of wild-type chaperonin GroEL.
J Mol Biol. 2005 Dec 9;354(4):940-51. doi: 10.1016/j.jmb.2005.09.096. Epub 2005 Oct 21.
2
Allosteric regulation of chaperonins.
Curr Opin Struct Biol. 2005 Dec;15(6):646-51. doi: 10.1016/j.sbi.2005.10.001. Epub 2005 Oct 24.
3
The unfolding action of GroEL on a protein substrate.
Biophys J. 2004 Jul;87(1):562-73. doi: 10.1529/biophysj.103.037333.
4
ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.
J Mol Biol. 1965 May;12:88-118. doi: 10.1016/s0022-2836(65)80285-6.
5
Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding.
Adv Protein Chem. 2001;59:45-72. doi: 10.1016/s0065-3233(01)59002-6.
6
Stimulation of the weak ATPase activity of human hsp90 by a client protein.
J Mol Biol. 2002 Jan 25;315(4):787-98. doi: 10.1006/jmbi.2001.5245.
7
ATP-bound states of GroEL captured by cryo-electron microscopy.
Cell. 2001 Dec 28;107(7):869-79. doi: 10.1016/s0092-8674(01)00617-1.
8
Differing ADP release rates from myosin heavy chain isoforms define the shortening velocity of skeletal muscle fibers.
J Biol Chem. 2001 Dec 7;276(49):45902-8. doi: 10.1074/jbc.M107434200. Epub 2001 Oct 5.
9
Review: allostery in chaperonins.
J Struct Biol. 2001 Aug;135(2):104-14. doi: 10.1006/jsbi.2001.4377.
10
Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP.
Biochim Biophys Acta. 2001 Feb 9;1545(1-2):160-73. doi: 10.1016/s0167-4838(00)00274-0.
Zotero 插件